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Three‐dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus.
Author(s) -
AEvarsson A.,
Brazhnikov E.,
Garber M.,
Zheltonosova J.,
Chirgadze Y.,
alKaradaghi S.,
Svensson L.A.,
Liljas A.
Publication year - 1994
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1994.tb06676.x
Subject(s) - thermus thermophilus , library science , biology , computer science , genetics , escherichia coli , gene
The crystal structure of Thermus thermophilus elongation factor G without guanine nucleotide was determined to 2.85 A. This GTPase has five domains with overall dimensions of 50 × 60 × 118 A. The GTP binding domain has a core common to other GTPases with a unique subdomain which probably functions as an intrinsic nucleotide exchange factor. Domains I and II are homologous to elongation factor Tu and their arrangement, both with and without GDP, is more similar to elongation factor Tu in complex with a GTP analogue than with GDP. Domains III and V show structural similarities to ribosomal proteins. Domain IV protrudes from the main body of the protein and has an extraordinary topology with a left‐handed cross‐over connection between two parallel beta‐strands.